GlcN6P deaminase is an allosteric enzyme and kinetic evidence shows that it undergoes a concerted allosteric transition. The current knowledge about the kinetics of this enzyme and its easy expression and purification indicate that GlcN6P deaminase may be a useful system for the study of allosteric transitions. A main interest in these results derives from enhancing the resolution to be able to determine the conformation of a particular motif of 30 aminoacids linking the allosteric and the active sites. The conformation of this structural part seems to be responsible for the activation of the enzyme and resulted partially disordered in the present structure. SR should provide information on the conformation of this motif which can be essential for the understanding of the allosteric mechanism of this enzyme.